β-Lactoglobulin mutant Lys69Asn has attenuated IgE and increased retinol binding activity

Journal of Biotechnology

Volumn 212, Issue , 2015, Pages 181-188

  Taheri Kafrani, Asghar ^a   Tavakkoli Koupaie, Neda ^a   Haertlé, Thomas ^b  

^a UNIVERSITY OF ISFAHAN   (Iran)

^b INRA   (France)

Author keywords

Competitive ELISA; Cow's milk allergy; Immunoreactivity; Ligand binding; Mutation; Lactoglobulin

Indexed keywords

ALLERGENS; AMINO ACIDS; ANTIBODIES; DAIRY PRODUCTS; DICHROISM; FATTY ACIDS; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES; PALMITIC ACID; PROTEINS; YEAST;

COMPETITIVE ELISA; IMMUNOREACTIVITIES; LACTOGLOBULIN; LIGAND BINDING; MILK ALLERGIES; MUTATION;

ALLERGIES;

ASPARAGINE; BETA LACTOGLOBULIN; EPITOPE; IMMUNOGLOBULIN E; LYSINE; LYSINE AT POSITION 69 ASPARAGINE; PALMITIC ACID; RECOMBINANT PROTEIN; RESVERATROL; RETINOL; SEROTONIN; TRYPTOPHAN; UNCLASSIFIED DRUG; IMMUNOGLOBULIN G; LACTOGLOBULIN; MONOCLONAL ANTIBODY; PROTEIN BINDING; STILBENE DERIVATIVE;

ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CLINICAL ARTICLE; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HUMAN; KOMAGATAELLA PASTORIS; MASS SPECTROMETRY; MILK ALLERGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; WILD TYPE; BLOOD; GENETICS; IMMUNOLOGY; METABOLISM; MUTATION; PICHIA;

ANTIBODIES, MONOCLONAL; ASPARAGINE; HUMANS; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; LACTOGLOBULINS; LYSINE; MILK HYPERSENSITIVITY; MUTATION; PALMITIC ACID; PICHIA; PROTEIN BINDING; STILBENES; VITAMIN A;

EID: 84942058308     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2015.08.006     Document Type: Article

References (60)

1. Belatik A., Hotchandani S., Bariyanga J., Tajmir-Riahi H.A. Binding sites of retinol and retinoic acid with serum albumins. Eur. J. Med. Chem. 2012, 48:114-123.
2. Benedé S., López-Expósito I., Giménez G., Grishina G., Bardina L., Sampson H.A., López-Fandiño R., Molina E. Mapping of IgE epitopes in in vitro gastroduodenal digests of β-lactoglobulin produced with human and simulated fluids. Food Res. Int. 2014, 62:1127-1133.
3. Burks W., Ballmer-Weber B.K. Food allergy. Mol. Nutr. Food Res. 2006, 50:595-603.
4. Chafen J.J.S., Newberry S.J., Riedl M.A., Bravata D.M., Maglione M., Suttorp M.J., Sundaram V., Paige N.M., Towfigh A., Hulley B.J. Diagnosing and managing common food allergies: a systematic review. J. Am. Med. Assoc. 2010, 303:1848-1856.
5. Cogan U., Kopelman M., Mokady S., Shinitzky M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 1976, 65:71-78.
6. Collini M., D'Alfonso L., Baldini G. New insight on β-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Sci. 2000, 9:1968-1974.
7. De Wolf F.A., Brett G.M. Ligand-binding proteins: their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol. Rev. 2000, 52:207-236.
8. Diarrassouba F., Garrait G., Remondetto G., Alvarez P., Beyssac E., Subirade M. Increased stability and protease resistance of the β-lactoglobulin/vitamin D 3 complex. Food chem. 2014, 145:646-652.
9. Ebeler S., Phillips L., Kinsella J. Purification of β-lactoglobulin: Isolation of genetic variants and influence of purification method on secondary structure. Milchwissenschaft 1990, 45:694-698.
10. El Mecherfi K.E., Rouaud O., Curet S., Negaoui H., Chobert J.M., Kheroua O., Saidi D., Haertlé T. Peptic hydrolysis of bovine beta-lactoglobulin under microwave treatment reduces its allergenicity in an ex vivo murine allergy model. Int. J. Food Sci. Technol. 2015, 50:356-364.
11. Ferreira F., Briza P., Infuhr D., Schmidt G., Wallner M., Wopfner N., Thalhamer J., Achatz G. Modified recombinant allergens for safer immunotherapy. Inflam. Allergy Drug Targets 2006, 5:5-14.
12. Fogolari F., Ragona L., Zetta L., Romagnoli S., De Kruif K.G., Molinari H. Monomeric bovine beta-lactoglobulin adopts a beta barrel fold at pH 2. FEBS Lett. 1998, 436:149-154.
13. Fuquay J.W., Fox P.F., McSweeney P.L. Encyclopedia of Dairy Sciences. 2011, Academic Press. 2nd Ed.
14. Furrie E. Probiotics and allergy. Proc. Nutr. Soc. 2005, 64:465-469.
15. Høst A. Frequency of cow's milk allergy in childhood. Ann. Allergy Asthma Immunol. 2002, 89:33-37.
16. Hambling S.G., McAlpine A.S., Sawyer L., Fox P. β-Lactoglobulin. Adv. Dairy Chem. 1 protein 1992, 2:141-190.
17. Hosking C., Heine R., Hill D. The Melbourne milk allergy study-two decades of clinical research. ACI International 2000, 12:198-205.
18. Hu Y.-J., Liu Y., Wang J.-B., Xiao X.-H., Qu S.-S. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J. Pharm. Biomed. Anal. 2004, 36:915-919.
19. Jaer L., Wuthrich B. Food Allergies and Intolerances (in German) 1998, Gustav Fischer Verlag, Ulm, Germany. 1st ed.
20. Kalach N., Rocchiccioli F., Boissieu D., Benhamou P.H., Dupont C. Intestinal permeability in children: variation with age and reliability in the diagnosis of cow's milk allergy. Acta Paediatr 2001, 90:499-504.
21. Kim T.-R., Goto Y., Hirota N., Kuwata K., Denton H., Wu S.-Y., Sawyer L., Batt C.A. High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein eng 1997, 10:1339-1345.
22. Kontopidis G., Holt C., Sawyer L. β-Lactoglobulin: binding properties, structure, and function. J. Dairy Sci. 2004, 87:785-796.
23. Laemmli U.K. Most commonly used discontinuous buffer system for SDS electrophoresis. Nature 1970, 227:680-685.
24. Lakowicz J.R. Principles of fluorescence spectroscopy 2006, New York. 3rd Ed.
25. Le Maux S., Bouhallab S., Giblin L., Brodkorb A., Croguennec T.B., ovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties. Dairy Sci. Technol. 2014, 94:409-426.
26. Li M., Ma Y., Ngadi M.O. Binding of curcumin to β-lactoglobulin and its effect on antioxidant characteristics of curcumin. Food chem. 2013, 141:1504-1511.
27. Liang L., Subirade M. β-Lactoglobulin/folic acid complexes: Formation, characterization, and biological implication. J. Phys. Chem. B 2010, 114:6707-6712.
28. Liang L., Subirade M. Study of the acid and thermal stability of β-lactoglobulin-ligand complexes using fluorescence quenching. Food Chem. 2012, 132:2023-2029.
29. Liang L., Tajmir-Riahi H., Subirade M. Interaction of β-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 2007, 9:50-56.
30. Linhart B., Valenta R. Molecular design of allergy vaccines. Curr. Opin. Immunol. 2005, 17:646-655.
31. Mailliart P., Ribadeau Dumas B. Preparation of β-lactoglobulin and p-lactoglobulin-free proteins from whey retentate by NaCI salting out at low pH. J. Food Sci. 1988, 53:743-745.
32. Mensi A., Choiset Y., Rabesona H., Haertlé T., Borel P., Chobert J.M. Interactions of í-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids. J. Agric. Food Chem. 2013, 61:4114-4119.
33. Mills E., Valovirta E., Madsen C., Taylor S., Vieths S., Anklam E., Baumgartner S., Koch P., Crevel R., Frewer L. Information provision for allergic consumers-where are we going with food allergen labelling?. Allergy 2004, 59:1262-1268.
34. Nakazawa T., Takai T., Hatanaka H., Mizuuchi E., Nagamune T., Okumura K., Ogawa H. Multiple-mutation at a potential ligand-binding region decreased allergenicity of a mite allergen Der f 2 without disrupting global structure. FEBS Lett 2005, 579:1988-1994.
35. Paul B.K., Ghosh N., Mukherjee S. Binding Interaction of a Prospective Chemotherapeutic Antibacterial Drug with β-Lactoglobulin: Results and Challenges. Langmuir 2014, 30:5921-5929.
36. Pescuma M., Hébert E.M., Haertlé T., Chobert J.-M., Mozzi F., Font de Valdez G. Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of é-lactoglobulin. Food Chem. 2015, 170:407-414.
37. Saarinen K.M., Pelkonen A.S., Mäkelä M.J., Savilahti E. Clinical course and prognosis of cow's milk allergy are dependent on milk-specific IgE status. J. Allergy Clin. Immunol. 2005, 116:869-875.
38. Sawyer L. β-Lactoglobulin. Adv. Dairy Chem. 2013, 211-259.
39. Schwartz H., Nerurkar L., Spies J., Scanlon R., Bellanti J. Milk hypersensitivity: RAST studies using new antigens generated by pepsin hydrolysis of beta-lactoglobulin. Ann. Allergy Asthma Immunol. 1980, 45:242-245.
40. Schwieger C., Ropers M.-H. Binding of a perfluorinated surfactant to β-lactoglobulin in aqueous solutions. Food Hydrocoll. 2013, 30:241-248.
41. Sicherer S.H., Sampson H.A. Food allergy. J. Allergy Clin. Immunol. 2010, 125:S116-S125.
42. Song C.Y., Chen W.L., Yang M.C., Huang J.P., Mao S.J. Epitope Mapping of a Monoclonal Antibody Specific to bovine dry milk involvement of residues 66-76 of strand D in thermal denatured β-lactoglobulin. J. Biol. Chem. 2005, 280:3574-3582.
43. Stanley J., Bannon G. Biochemistry of food allergens. Clin. Rev. Allergy Immunol. 1999, 17:279-291.
44. Taheri-Kafrani A., Bordbar A.K., Mousavi S.H.A., Haertlé T. β-Lactoglobulin structure and retinol binding changes in presence of anionic and neutral detergents. J. Agric. Food Chem. 2008, 56:7528-7534.
45. Taheri-Kafrani A., Gaudin J.C., Rabesona H., Nioi C., Agarwal D., Drouet M., Chobert J.-M., Bordbar A.-K., Haertle T. Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J. Agric. Food Chem. 2009, 57:4974-4982.
46. Taheri-Kafrani A., Asgari-Mobarakeh E., Bordbar A.K., Haertlé T. Structure-function relationship of β-lactoglobulin in the presence of dodecyltrimethyl ammonium bromide. Coll. Surf. B Biointerf. 2010, 75:268-274.
47. Taheri-Kafrani A., Choiset Y., Faizullin D.A., Zuev Y.F., Bezuglov V.V., Chobert J.M., Bordbar A.K., Haertlé T. Interactions of β-lactoglobulin with serotonin and arachidonyl serotonin. Biopolymers 2011, 95:871-880.
48. Taylor S.L., Hefle S.L. Food allergies and other food sensitivities. Food Thechnol. 2001, 55:68-84.
49. Uhrínová S., Smith M.H., Jameson G.B., Uhrín D., Sawyer L., Barlow P.N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 2000, 39:3565-3574.
50. Valenta R., Vrtala S., Focke-Tejkl M., Bugajska-Schretter A., Ball T., Twardosz A., Spitzauer S., Grönlund H., Kraft D. Genetically engineered and synthetic allergen derivatives: candidates for vaccination against type I allergy. Biol. Chem. 1999, 380:815-824.
51. Valenta R., Ferreira F., Focke-Tejkl M., Linhart B., Niederberger V., Swoboda I., Vrtala S. From allergen genes to allergy vaccines. Annu. Rev. Immunol. 2009, 28:211-241.
52. Valenta R. The future of antigen-specific immunotherapy of allergy. Nat. Rev. Immunol. 2002, 2:446-453.
53. van Esch B.C., Knipping K., Jeurink P., van der Heide S., Dubois A.E., Willemsen L.E., Garssen J., Knippels L.M. In vivo and in vitro evaluation of the residual allergenicity of partially hydrolysed infant formulas. Toxicol. Lett. 2011, 201:264-269.
54. van Hengel A.J. Food allergen detection methods and the challenge to protect food-allergic consumers. Anal. Bioanal. Chem. 2007, 389:111-118.
55. Venien A., Levieux D., Astier C., Briand L., Chobert J.-M., Haertle T. Production and epitopic characterization of monoclonal antibodies against bovine β-lactoglobulin. J. Dairy sci. 1997, 80:1977-1987.
56. Wal J.M. Cow's milk allergens. Allergy 1998, 53:1013-1022.
57. Wal J.M. Bovine milk allergenicity. Ann. Allergy Asthma Immunol. 2004, 93:S2-S11.
58. Wilson C., Quarrie L., Allan G.J., Flint D.J., Sawyer L., Holt C. Expression of recombinant wild-type and mutant β-Lactoglobulins in the yeast Pichia pastoris. Int. J. Food Sci. Technol. 1999, 34:445-450.
59. Yang M.C., Guan H.H., Liu M.Y., Lin Y.H., Yang J.M., Chen W.L., Chen C.J., Mao S.J. Crystal structure of a secondary vitamin D3 binding site of milk β-lactoglobulin. Proteins 2008, 71:1197-1210.
60. Zhong J., Tu Y., Liu W., Xu Y., Liu C., Dun R. Antigenicity and conformational changes of β-lactoglobulin by dynamic high pressure microfluidization combining with glycation treatment. J. Dairy Sci. 2014, 97:4695-4702.